ID   KIF22_PONAB             Reviewed;         665 AA.
AC   Q5REP4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Kinesin-like protein KIF22;
GN   Name=KIF22;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Kinesin family member that is involved in spindle formation
CC       and the movements of chromosomes during mitosis and meiosis. Binds to
CC       microtubules and to DNA. Plays a role in congression of laterally
CC       attached chromosomes in NDC80-depleted cells.
CC       {ECO:0000250|UniProtKB:Q14807, ECO:0000250|UniProtKB:Q9I869}.
CC   -!- SUBUNIT: Interacts with FAM83D and SIAH1.
CC       {ECO:0000250|UniProtKB:Q14807}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14807}.
CC       Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent
CC       proteasomal degradation. {ECO:0000250|UniProtKB:Q14807}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR   EMBL; CR857477; CAH89763.1; -; mRNA.
DR   RefSeq; NP_001128749.1; NM_001135277.1.
DR   AlphaFoldDB; Q5REP4; -.
DR   SMR; Q5REP4; -.
DR   STRING; 9601.ENSPPYP00000008681; -.
DR   PRIDE; Q5REP4; -.
DR   Ensembl; ENSPPYT00000009034; ENSPPYP00000008681; ENSPPYG00000007701.
DR   GeneID; 100189644; -.
DR   KEGG; pon:100189644; -.
DR   CTD; 3835; -.
DR   eggNOG; KOG0242; Eukaryota.
DR   GeneTree; ENSGT00940000159632; -.
DR   HOGENOM; CLU_001485_27_1_1; -.
DR   InParanoid; Q5REP4; -.
DR   OMA; VIREDRW; -.
DR   OrthoDB; 787964at2759; -.
DR   TreeFam; TF105233; -.
DR   Proteomes; UP000001595; Chromosome 16.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR   GO; GO:0007062; P:sister chromatid cohesion; ISS:UniProtKB.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR026986; KIF22.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010994; RuvA_2-like.
DR   PANTHER; PTHR24115; PTHR24115; 1.
DR   PANTHER; PTHR24115:SF801; PTHR24115:SF801; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00278; HhH1; 2.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; DNA-binding;
KW   Isopeptide bond; Microtubule; Motor protein; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..665
FT                   /note="Kinesin-like protein KIF22"
FT                   /id="PRO_0000262922"
FT   DOMAIN          43..368
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          465..508
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        394..410
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         127..134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14807"
FT   MOD_RES         427
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14807"
FT   MOD_RES         452
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14807"
FT   MOD_RES         543
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14807"
FT   MOD_RES         562
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14807"
FT   MOD_RES         581
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14807"
FT   CROSSLNK        465
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q14807"
SQ   SEQUENCE   665 AA;  73365 MW;  5D058AF12D500E15 CRC64;
     MAAEGSTQQR RRVMAAASAA STSGAGRCRL SKIGASRRPP PARVRVAVRL RPFVDGTAGA
     SDPPCVRGMD SCSLEIANWR NHQETLKYQF DAFYGERSTQ QDIYAGSVQP ILRHLLEGQN
     ASVLAYGPTG AGKTHTMLGS PEQPGVIPRA LMDLLQLTRE EGAEGRPWAL SVTMSYLEIY
     QEKVLDLLDP ASGDLVIRED CRGNILIPGL TQKPITSFAD FERHFLPASR NRTVGATRLN
     QRSSRSHAVL LVKVDQRERL APFRQREGKL YLIDLAGSED NRRTGNKGLR LKESGAINTS
     LFVLGKVVDA LNQGLPRVPY RDSKLTRLLQ DSLGGSAHSI LIANIAPERC FYLDTVSALN
     FAARSKEVIN RPFTNESLQP HVLGPVKLSQ KELLGPPEAK RARGPEEEEI GSPEPMAAPA
     SASQKLSPLQ KLSSMDPAML ERLLSLDRLL ASQGSQGAPL LSTPKRERMV LMKTVEEKDL
     EIERLKTKQK ELEAKMLAQK AEEKENHCPT MLRPLSHRTV TVAKPLKKAV VMPLQLIQEQ
     AASPNAEIHI LKNKGRKRKL ESLDALEPEE KAEDCWELQI SPELLAHGRQ KILDLLNEGS
     ARDLRSLQRI GPKKAQLIVG WRELHGPFSQ VEDLERVEGI TGKQMESFLK ANILGLAAGQ
     RCGPS